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Volumn 393, Issue , 2005, Pages 394-408

Analyzing the degradation of PERIOD protein by the ubiquitin-proteasome pathway in cultured Drosophila cells

Author keywords

[No Author keywords available]

Indexed keywords

PER1 PROTEIN; PROTEASOME; UBIQUITIN;

EID: 16844381705     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(05)93018-8     Document Type: Article
Times cited : (8)

References (70)
  • 1
    • 0036178045 scopus 로고    scopus 로고
    • Control of intracellular dynamics of mammalian period proteins by casein kinase I epsilon (CKIepsilon) and CKIdelta in cultured cells
    • Akashi M., Tsuchiya Y., Yoshino T., Nishida E. Control of intracellular dynamics of mammalian period proteins by casein kinase I epsilon (CKIepsilon) and CKIdelta in cultured cells. Mol. Cell. Biol. 22:2002;1693-1703
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1693-1703
    • Akashi, M.1    Tsuchiya, Y.2    Yoshino, T.3    Nishida, E.4
  • 3
    • 0025910282 scopus 로고
    • Comparison of several promoters and polyadenylation signals for use in heterologous gene expression in cultured Drosophila cells
    • Angelichio M.L., Beck J.A., Johansen H., Ivey-Hoyle M. Comparison of several promoters and polyadenylation signals for use in heterologous gene expression in cultured Drosophila cells. Nucleic Acids Res. 19:1991;5037-5043
    • (1991) Nucleic Acids Res. , vol.19 , pp. 5037-5043
    • Angelichio, M.L.1    Beck, J.A.2    Johansen, H.3    Ivey-Hoyle, M.4
  • 5
    • 0032511229 scopus 로고    scopus 로고
    • A serum shock induces circadian gene expression in mammalian tissue culture cells
    • Balsalobre A., Damiola F., Schibler U. A serum shock induces circadian gene expression in mammalian tissue culture cells. Cell. 93:1998;929-937
    • (1998) Cell , vol.93 , pp. 929-937
    • Balsalobre, A.1    Damiola, F.2    Schibler, U.3
  • 6
    • 0024284041 scopus 로고
    • Characterization and use of the Drosophila metallothionein promoter in cultured Drosophila melanogaster cells
    • Bunch T.A., Grinblat Y., Goldstein L.S. Characterization and use of the Drosophila metallothionein promoter in cultured Drosophila melanogaster cells. Nucleic Acids Res. 16:1988;1043-1061
    • (1988) Nucleic Acids Res. , vol.16 , pp. 1043-1061
    • Bunch, T.A.1    Grinblat, Y.2    Goldstein, L.S.3
  • 8
    • 0038032878 scopus 로고    scopus 로고
    • A novel C-terminal domain of drosophila PERIOD inhibits dCLOCK:CYCLE-mediated transcription
    • Chang D.C., Reppert S.M. A novel C-terminal domain of drosophila PERIOD inhibits dCLOCK:CYCLE-mediated transcription. Curr. Biol. 13:2003;758-762
    • (2003) Curr. Biol. , vol.13 , pp. 758-762
    • Chang, D.C.1    Reppert, S.M.2
  • 12
    • 0034065822 scopus 로고    scopus 로고
    • Ubiquitin-mediated proteolysis: Biological regulation via destruction
    • Ciechanover A., Orian A., Schwartz A.L. Ubiquitin-mediated proteolysis: Biological regulation via destruction. Bioessays. 22:2000;442-451
    • (2000) Bioessays , vol.22 , pp. 442-451
    • Ciechanover, A.1    Orian, A.2    Schwartz, A.L.3
  • 13
    • 0033453239 scopus 로고    scopus 로고
    • Attenuation of green fluorescent protein half-life in mammalian cells
    • Corish P., Tyler-Smith C. Attenuation of green fluorescent protein half-life in mammalian cells. Protein Eng. 12:1999;1035-1040
    • (1999) Protein Eng. , vol.12 , pp. 1035-1040
    • Corish, P.1    Tyler-Smith, C.2
  • 14
    • 0032860066 scopus 로고    scopus 로고
    • The F-box: A new motif for ubiquitin dependent proteolysis in cell cycle regulation and signal transduction
    • Craig K.L., Tyers M. The F-box: A new motif for ubiquitin dependent proteolysis in cell cycle regulation and signal transduction. Prog. Biophys. Mol. Biol. 72:1999;299-328
    • (1999) Prog. Biophys. Mol. Biol. , vol.72 , pp. 299-328
    • Craig, K.L.1    Tyers, M.2
  • 16
    • 0034463801 scopus 로고    scopus 로고
    • The period E-box is sufficient to drive circadian oscillation of transcription in vivo
    • Darlington T.K., Lyons L.C., Hardin P.E., Kay S.A. The period E-box is sufficient to drive circadian oscillation of transcription in vivo. J. Biol. Rhythms. 15:2000;462-471
    • (2000) J. Biol. Rhythms , vol.15 , pp. 462-471
    • Darlington, T.K.1    Lyons, L.C.2    Hardin, P.E.3    Kay, S.A.4
  • 17
    • 0033593306 scopus 로고    scopus 로고
    • Molecular bases for circadian clocks
    • Dunlap J.C. Molecular bases for circadian clocks. Cell. 96:1999;271-290
    • (1999) Cell , vol.96 , pp. 271-290
    • Dunlap, J.C.1
  • 19
    • 0032805313 scopus 로고    scopus 로고
    • Role of posttranscriptional regulation in circadian clocks: Lessons from Drosophila
    • Edery I. Role of posttranscriptional regulation in circadian clocks: Lessons from Drosophila. Chronobiol. Int. 16:1999;377-414
    • (1999) Chronobiol. Int. , vol.16 , pp. 377-414
    • Edery, I.1
  • 20
    • 0032567038 scopus 로고    scopus 로고
    • CRY, a Drosophila clock and light-regulated cryptochrome, is a major contributor to circadian rhythm resetting and photosensitivity
    • Emery P., So W.V., Kaneko M., Hall J.C., Rosbash M. CRY, a Drosophila clock and light-regulated cryptochrome, is a major contributor to circadian rhythm resetting and photosensitivity. Cell. 95:1998;669-679
    • (1998) Cell , vol.95 , pp. 669-679
    • Emery, P.1    So, W.V.2    Kaneko, M.3    Hall, J.C.4    Rosbash, M.5
  • 21
    • 0031001092 scopus 로고    scopus 로고
    • Identification of a Drosophila melanogaster ICE/CED-3-related protease, drICE
    • Fraser A.G., Evan G.I. Identification of a Drosophila melanogaster ICE/CED-3-related protease, drICE. EMBO J. 16:1997;2805-2813
    • (1997) EMBO J. , vol.16 , pp. 2805-2813
    • Fraser, A.G.1    Evan, G.I.2
  • 22
    • 0035975923 scopus 로고    scopus 로고
    • Perspectives of immobilized-metal affinity chromatography
    • Gaberc-Porekar V., Menart V. Perspectives of immobilized-metal affinity chromatography. J. Biochem. Biophys. Methods. 49:2001;335-360
    • (2001) J. Biochem. Biophys. Methods , vol.49 , pp. 335-360
    • Gaberc-Porekar, V.1    Menart, V.2
  • 23
    • 0031006674 scopus 로고    scopus 로고
    • Alternative initiation of translation and time-specific phosphorylation yield multiple forms of the essential clock protein FREQUENCY
    • Garceau N.Y., Liu Y., Loros J.J., Dunlap J.C. Alternative initiation of translation and time-specific phosphorylation yield multiple forms of the essential clock protein FREQUENCY. Cell. 89:1997;469-476
    • (1997) Cell , vol.89 , pp. 469-476
    • Garceau, N.Y.1    Liu, Y.2    Loros, J.J.3    Dunlap, J.C.4
  • 24
    • 0037126627 scopus 로고    scopus 로고
    • A PEST-like element in FREQUENCY determines the length of the circadian period in Neurospora crassa
    • Gorl M., Merrow M., Huttner B., Johnson J., Roenneberg T., Brunner M. A PEST-like element in FREQUENCY determines the length of the circadian period in Neurospora crassa. EMBO J. 20:2001;7074-7084
    • (2001) EMBO J. , vol.20 , pp. 7074-7084
    • Gorl, M.1    Merrow, M.2    Huttner, B.3    Johnson, J.4    Roenneberg, T.5    Brunner, M.6
  • 25
    • 0025360747 scopus 로고
    • A uniform isopeptide-linked multiubiquitin chain is sufficient to target substrate for degradation in ubiquitin-mediated proteolysis
    • Gregori L., Poosch M.S., Cousins G., Chau V. A uniform isopeptide-linked multiubiquitin chain is sufficient to target substrate for degradation in ubiquitin-mediated proteolysis. J. Biol. Chem. 265:1990;8354-8357
    • (1990) J. Biol. Chem. , vol.265 , pp. 8354-8357
    • Gregori, L.1    Poosch, M.S.2    Cousins, G.3    Chau, V.4
  • 26
    • 0037079034 scopus 로고    scopus 로고
    • The F-box protein slimb controls the levels of clock proteins period and timeless
    • Grima B., Lamouroux A., Chelot E., Papin C., Limbourg-Bouchon B., Rouyer F. The F-box protein slimb controls the levels of clock proteins period and timeless. Nature. 420:2002;178-182
    • (2002) Nature , vol.420 , pp. 178-182
    • Grima, B.1    Lamouroux, A.2    Chelot, E.3    Papin, C.4    Limbourg-Bouchon, B.5    Rouyer, F.6
  • 27
    • 0042237024 scopus 로고    scopus 로고
    • FWD1-mediated degradation of FREQUENCY in Neurospora establishes a conserved mechanism for circadian clock regulation
    • He Q., Cheng P., Yang Y., Yu H., Liu Y. FWD1-mediated degradation of FREQUENCY in Neurospora establishes a conserved mechanism for circadian clock regulation. EMBO J. 22:2003;4421-4430
    • (2003) EMBO J. , vol.22 , pp. 4421-4430
    • He, Q.1    Cheng, P.2    Yang, Y.3    Yu, H.4    Liu, Y.5
  • 28
    • 0035542874 scopus 로고    scopus 로고
    • Applications of novel affinity cassette methods: Use of peptide fusion handles for the purification of recombinant proteins
    • Hearn M.T., Acosta D. Applications of novel affinity cassette methods: Use of peptide fusion handles for the purification of recombinant proteins. J. Mol. Recogn. 14:2001;323-369
    • (2001) J. Mol. Recogn. , vol.14 , pp. 323-369
    • Hearn, M.T.1    Acosta, D.2
  • 29
    • 0023659137 scopus 로고
    • New metal chelate adsorbent selective for proteins and peptides containing neighbouring histidine residues
    • Hochuli E., Dobeli H., Schacher A. New metal chelate adsorbent selective for proteins and peptides containing neighbouring histidine residues. J. Chromatogr. 411:1987;177-184
    • (1987) J. Chromatogr. , vol.411 , pp. 177-184
    • Hochuli, E.1    Dobeli, H.2    Schacher, A.3
  • 30
    • 0344443180 scopus 로고    scopus 로고
    • FKF1 is essential for photoperiodic-specific light signalling in Arabidopsis
    • Imaizumi T., Tran H.G., Swartz T.E., Briggs W.R., Kay S.A. FKF1 is essential for photoperiodic-specific light signalling in Arabidopsis. Nature. 426:2003;302-306
    • (2003) Nature , vol.426 , pp. 302-306
    • Imaizumi, T.1    Tran, H.G.2    Swartz, T.E.3    Briggs, W.R.4    Kay, S.A.5
  • 31
    • 0024688637 scopus 로고
    • Regulated expression at high copy number allows production of a growth-inhibitory oncogene product in Drosophila Schneider cells
    • Johansen H., van der Straten A., Sweet R., Otto E., Maroni G., Rosenberg M. Regulated expression at high copy number allows production of a growth-inhibitory oncogene product in Drosophila Schneider cells. Genes Dev. 3:1989;882-889
    • (1989) Genes Dev. , vol.3 , pp. 882-889
    • Johansen, H.1    Van Der Straten, A.2    Sweet, R.3    Otto, E.4    Maroni, G.5    Rosenberg, M.6
  • 32
    • 0001619410 scopus 로고    scopus 로고
    • Phosphorylation and destabilization of human period I clock protein by human casein kinase I epsilon
    • Keesler G.A., Camacho F., Guo Y., Virshup D., Mondadori C., Yao Z. Phosphorylation and destabilization of human period I clock protein by human casein kinase I epsilon. Neuroreport. 11:2000;951-955
    • (2000) Neuroreport , vol.11 , pp. 951-955
    • Keesler, G.A.1    Camacho, F.2    Guo, Y.3    Virshup, D.4    Mondadori, C.5    Yao, Z.6
  • 33
    • 0037447277 scopus 로고    scopus 로고
    • Circadian phase-specific degradation of the F-box protein ZTL is mediated by the proteasome
    • Kim W.Y., Geng R., Somers D.E. Circadian phase-specific degradation of the F-box protein ZTL is mediated by the proteasome. Proc. Natl. Acad. Sci. USA. 100:2003;4933-4938
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4933-4938
    • Kim, W.Y.1    Geng, R.2    Somers, D.E.3
  • 34
    • 0034568688 scopus 로고    scopus 로고
    • The F-box protein family
    • REVIEWS 3002
    • Kipreos E.T., Pagano M. The F-box protein family. Genome Biol. 1:2000;. REVIEWS 3002
    • (2000) Genome Biol. , vol.1
    • Kipreos, E.T.1    Pagano, M.2
  • 35
    • 0032504041 scopus 로고    scopus 로고
    • The Drosophila clock gene double-time encodes a protein closely related to human casein kinase Iε
    • Kloss B., Price J.L., Saez L., Blau J., Rothenfluh A., Wesley C.S., Young M.W. The Drosophila clock gene double-time encodes a protein closely related to human casein kinase Iε Cell. 94:1998;97-107
    • (1998) Cell , vol.94 , pp. 97-107
    • Kloss, B.1    Price, J.L.2    Saez, L.3    Blau, J.4    Rothenfluh, A.5    Wesley, C.S.6    Young, M.W.7
  • 36
    • 0034964474 scopus 로고    scopus 로고
    • Phosphorylation of period is influenced by cycling physical associations of double-time, period, and timeless in the Drosophila clock
    • Kloss B., Rothenfluh A., Young M.W., Saez L. Phosphorylation of period is influenced by cycling physical associations of double-time, period, and timeless in the Drosophila clock. Neuron. 30:2001;699-706
    • (2001) Neuron , vol.30 , pp. 699-706
    • Kloss, B.1    Rothenfluh, A.2    Young, M.W.3    Saez, L.4
  • 37
    • 0037069671 scopus 로고    scopus 로고
    • Role for Slimb in the degradation of Drosophila Period protein phosphorylated by Doubletime
    • Ko H.W., Jiang J., Edery I. Role for Slimb in the degradation of Drosophila Period protein phosphorylated by Doubletime. Nature. 420:2002;673-678
    • (2002) Nature , vol.420 , pp. 673-678
    • Ko, H.W.1    Jiang, J.2    Edery, I.3
  • 38
    • 0042626226 scopus 로고    scopus 로고
    • BMAL1-dependent circadian oscillation of nuclear CLOCK: Posttranslational events induced by dimerization of transcriptional activators of the mammalian clock system
    • Kondratov R.V., Chernov M.V., Kondratova A.A., Gorbacheva V.Y., Gudkov A.V., Antoch M.P. BMAL1-dependent circadian oscillation of nuclear CLOCK: Posttranslational events induced by dimerization of transcriptional activators of the mammalian clock system. Genes Dev. 17:2003;1921-1932
    • (2003) Genes Dev. , vol.17 , pp. 1921-1932
    • Kondratov, R.V.1    Chernov, M.V.2    Kondratova, A.A.3    Gorbacheva, V.Y.4    Gudkov, A.V.5    Antoch, M.P.6
  • 39
    • 0024313337 scopus 로고
    • Transcriptional activation and repression by Ultrabithorax proteins in cultured Drosophila cells
    • Krasnow M.A., Saffman E.E., Kornfeld K., Hogness D.S. Transcriptional activation and repression by Ultrabithorax proteins in cultured Drosophila cells. Cell. 57:1989;1031-1043
    • (1989) Cell , vol.57 , pp. 1031-1043
    • Krasnow, M.A.1    Saffman, E.E.2    Kornfeld, K.3    Hogness, D.S.4
  • 41
    • 0000870917 scopus 로고    scopus 로고
    • Selective inhibitors of the proteasome-dependent and vacuolar pathways of protein degradation in Saccharomyces cerevisiae
    • Lee D.H., Goldberg A.L. Selective inhibitors of the proteasome-dependent and vacuolar pathways of protein degradation in Saccharomyces cerevisiae. J. Biol. Chem. 271:1996;27280-27284
    • (1996) J. Biol. Chem. , vol.271 , pp. 27280-27284
    • Lee, D.H.1    Goldberg, A.L.2
  • 46
    • 0035875069 scopus 로고    scopus 로고
    • A role for the segment polarity gene shaggy/GSK-3 in the Drosophila circadian clock
    • Martinek S., Inonog S., Manoukian A.S., Young M.W. A role for the segment polarity gene shaggy/GSK-3 in the Drosophila circadian clock. Cell. 105:2001;769-779
    • (2001) Cell , vol.105 , pp. 769-779
    • Martinek, S.1    Inonog, S.2    Manoukian, A.S.3    Young, M.W.4
  • 47
    • 0348134861 scopus 로고    scopus 로고
    • Targeted degradation of TOC1 by ZTL modulates circadian function in Arabidopsis thaliana
    • Mas P., Kim W.Y., Somers D.E., Kay S.A. Targeted degradation of TOC1 by ZTL modulates circadian function in Arabidopsis thaliana. Nature. 426:2003;567-570
    • (2003) Nature , vol.426 , pp. 567-570
    • Mas, P.1    Kim, W.Y.2    Somers, D.E.3    Kay, S.A.4
  • 48
    • 0033543596 scopus 로고    scopus 로고
    • A role for the proteasome in the light response of the timeless clock protein
    • Naidoo N., Song W., Hunter-Ensor M., Sehgal A. A role for the proteasome in the light response of the timeless clock protein. Science. 285:1999;1737-1741
    • (1999) Science , vol.285 , pp. 1737-1741
    • Naidoo, N.1    Song, W.2    Hunter-Ensor, M.3    Sehgal, A.4
  • 49
    • 0442319504 scopus 로고    scopus 로고
    • The doubletime and CKII kinases collaborate to potentiate Drosophila PER transcriptional repressor activity
    • Nawathean P., Rosbash M. The doubletime and CKII kinases collaborate to potentiate Drosophila PER transcriptional repressor activity. Mol. Cell. 13:2004;213-223
    • (2004) Mol. Cell , vol.13 , pp. 213-223
    • Nawathean, P.1    Rosbash, M.2
  • 50
    • 0034724516 scopus 로고    scopus 로고
    • FKF1, a clock-controlled gene that regulates the transition to flowering in Arabidopsis
    • Nelson D.C., Lasswell J., Rogg L.E., Cohen M.A., Bartel B. FKF1, a clock-controlled gene that regulates the transition to flowering in Arabidopsis. Cell. 101:2000;331-340
    • (2000) Cell , vol.101 , pp. 331-340
    • Nelson, D.C.1    Lasswell, J.2    Rogg, L.E.3    Cohen, M.A.4    Bartel, B.5
  • 51
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart C.M. Mechanisms underlying ubiquitination. Annu. Rev. Biochem. 70:2001;503-533
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 52
    • 0032503969 scopus 로고    scopus 로고
    • Double-time is a novel Drosophila clock gene that regulates PERIOD protein accumulation
    • Price J.L., Blau J., Rothenfluh A., Abodeely M., Kloss B., Young M.W. double-time is a novel Drosophila clock gene that regulates PERIOD protein accumulation. Cell. 94:1998;83-95
    • (1998) Cell , vol.94 , pp. 83-95
    • Price, J.L.1    Blau, J.2    Rothenfluh, A.3    Abodeely, M.4    Kloss, B.5    Young, M.W.6
  • 53
    • 0021859522 scopus 로고
    • Transformation of cultured Drosophila melanogaster cells with a dominant selectable marker
    • Rio D.C., Rubin G.M. Transformation of cultured Drosophila melanogaster cells with a dominant selectable marker. Mol. Cell Biol. 5:1985;1833-1838
    • (1985) Mol. Cell Biol. , vol.5 , pp. 1833-1838
    • Rio, D.C.1    Rubin, G.M.2
  • 54
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • Rock K.L., Gramm C., Rothstein L., Clark K., Stein R., Dick L., Hwang D., Goldberg A.L. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell. 78:1994;761-771
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Hwang, D.7    Goldberg, A.L.8
  • 55
    • 0030293638 scopus 로고    scopus 로고
    • Regulation of nuclear entry of the Drosophila clock proteins period and timeless
    • Saez L., Young M.W. Regulation of nuclear entry of the Drosophila clock proteins period and timeless. Neuron. 17:1996;911-920
    • (1996) Neuron , vol.17 , pp. 911-920
    • Saez, L.1    Young, M.W.2
  • 56
    • 1342285689 scopus 로고    scopus 로고
    • Posttranslational regulation of Drosophila PERIOD protein by protein phosphatase 2A
    • Sathyanarayanan S., Zheng X., Xiao R., Sehgal A. Posttranslational regulation of Drosophila PERIOD protein by protein phosphatase 2A. Cell. 116:2004;603-615
    • (2004) Cell , vol.116 , pp. 603-615
    • Sathyanarayanan, S.1    Zheng, X.2    Xiao, R.3    Sehgal, A.4
  • 57
    • 0015328565 scopus 로고
    • Cell lines derived from late embryonic stages of Drosophila melanogaster
    • Schneider I. Cell lines derived from late embryonic stages of Drosophila melanogaster. J. Embryol. Exp. Morphol. 27:1972;353-365
    • (1972) J. Embryol. Exp. Morphol. , vol.27 , pp. 353-365
    • Schneider, I.1
  • 58
    • 0031948386 scopus 로고    scopus 로고
    • Differential effects of light and heat on the Drosophila circadian clock proteins PER and TIM
    • Sidote D., Majercak J., Parikh V., Edery I. Differential effects of light and heat on the Drosophila circadian clock proteins PER and TIM. Mol. Cell Biol. 18:1998;2004-2013
    • (1998) Mol. Cell Biol. , vol.18 , pp. 2004-2013
    • Sidote, D.1    Majercak, J.2    Parikh, V.3    Edery, I.4
  • 60
    • 0033231281 scopus 로고    scopus 로고
    • Degradation signals in the lysine-asparagine sequence space
    • Suzuki T., Varshavsky A. Degradation signals in the lysine-asparagine sequence space. EMBO J. 18:1999;6017-6026
    • (1999) EMBO J. , vol.18 , pp. 6017-6026
    • Suzuki, T.1    Varshavsky, A.2
  • 61
    • 0025823443 scopus 로고
    • Modulation of firefly luciferase stability and impact on studies of gene regulation
    • Thompson J.F., Hayes L.S., Lloyd D.B. Modulation of firefly luciferase stability and impact on studies of gene regulation. Gene. 103:1991;171-177
    • (1991) Gene , vol.103 , pp. 171-177
    • Thompson, J.F.1    Hayes, L.S.2    Lloyd, D.B.3
  • 62
    • 0024210345 scopus 로고
    • Vectors for Drosophila P-element-mediated transformation and tissue culture transfection
    • Thummel C.S., Boulet A.M., Lipshitz H.D. Vectors for Drosophila P-element-mediated transformation and tissue culture transfection. Gene. 74:1988;445-456
    • (1988) Gene , vol.74 , pp. 445-456
    • Thummel, C.S.1    Boulet, A.M.2    Lipshitz, H.D.3
  • 63
    • 0033995119 scopus 로고    scopus 로고
    • Proteolysis and the cell cycle: With this RING I do thee destroy
    • Tyers M., Jorgensen P. Proteolysis and the cell cycle: With this RING I do thee destroy. Curr. Opin. Genet Dev. 10:2000;54-64
    • (2000) Curr. Opin. Genet Dev. , vol.10 , pp. 54-64
    • Tyers, M.1    Jorgensen, P.2
  • 64
    • 0034045931 scopus 로고    scopus 로고
    • Nuclear entry of the circadian regulator mPER1 is controlled by mammalian casein kinase I epsilon
    • Vielhaber E., Eide E., Rivers A., Gao Z.H., Virshup D.M. Nuclear entry of the circadian regulator mPER1 is controlled by mammalian casein kinase I epsilon. Mol. Cell Biol. 20:2000;4888-4899
    • (2000) Mol. Cell Biol. , vol.20 , pp. 4888-4899
    • Vielhaber, E.1    Eide, E.2    Rivers, A.3    Gao, Z.H.4    Virshup, D.M.5
  • 65
    • 0035292759 scopus 로고    scopus 로고
    • Themes and variations on ubiquitylation
    • Weissman A.M. Themes and variations on ubiquitylation. Nature Rev. Mol. Cell. Biol. 2:2001;169-178
    • (2001) Nature Rev. Mol. Cell. Biol. , vol.2 , pp. 169-178
    • Weissman, A.M.1
  • 66
    • 0035860090 scopus 로고    scopus 로고
    • RNA interference of gene expression (RNAi) in cultured Drosophila cells
    • PL1
    • Worby C.A., Simonson-Leff N., Dixon J.E. RNA interference of gene expression (RNAi) in cultured Drosophila cells. Sci STKE 2001. 2001;. PL1
    • (2001) Sci STKE 2001
    • Worby, C.A.1    Simonson-Leff, N.2    Dixon, J.E.3
  • 67
    • 0037086535 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling and mCRY-dependent inhibition of ubiquitylation of the mPER2 clock protein
    • Yagita K., Tamanini F., Yasuda M., Hoeijmakers J.H., van der Horst G.T., Okamura H. Nucleocytoplasmic shuttling and mCRY-dependent inhibition of ubiquitylation of the mPER2 clock protein. EMBO J. 21:2002;1301-1314
    • (2002) EMBO J. , vol.21 , pp. 1301-1314
    • Yagita, K.1    Tamanini, F.2    Yasuda, M.3    Hoeijmakers, J.H.4    Van Der Horst, G.T.5    Okamura, H.6
  • 69
    • 0037089657 scopus 로고    scopus 로고
    • Regulation of the Neurospora circadian clock by casein kinase II
    • Yang Y., Cheng P., Liu Y. Regulation of the Neurospora circadian clock by casein kinase II. Genes Dev. 16:2002;994-1006
    • (2002) Genes Dev. , vol.16 , pp. 994-1006
    • Yang, Y.1    Cheng, P.2    Liu, Y.3
  • 70
    • 0035102288 scopus 로고    scopus 로고
    • Role of molecular oscillations in generating behavioral rhythms in Drosophila
    • Yang Z., Sehgal A. Role of molecular oscillations in generating behavioral rhythms in Drosophila. Neuron. 29:2001;453-467
    • (2001) Neuron , vol.29 , pp. 453-467
    • Yang, Z.1    Sehgal, A.2


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